FMO DATABASE

FMODB ID: ZNG3N

Calculation Name: 3F6N-A-Xray540

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 3F6N

Chain ID: A

ChEMBL ID:

UniProt ID: P03551

Base Structure: X-ray

Registration Date: 2025-07-08

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	136
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-275606.178913
FMO2-HF: Nuclear repulsion	248385.182731
FMO2-HF: Total energy	-27220.996182
FMO2-MP2: Total energy	-27298.650739

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:3:ASN)

Summations of interaction energy for fragment #1(A:3:ASN)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-4.061	-0.579	0.336	-1.686	-2.132	0.002

Interaction energy analysis for fragmet #1(A:3:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.215 / q_NPA : 0.094

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
4	A	4	LEU	0	-0.064	0.119	4.800	-0.095	0.132	-0.001	-0.102	-0.124	0.000
5	A	5	ASN	0	0.089	-0.079	3.596	-2.425	-0.951	0.020	-0.779	-0.715	0.003
6	A	5	ASN	0	-0.096	0.058	3.592	-0.518	-0.301	0.007	-0.105	-0.120	0.001
7	A	6	GLN	0	0.067	-0.102	2.945	-0.264	0.450	0.056	-0.257	-0.513	-0.002
8	A	6	GLN	0	-0.107	0.082	2.833	-0.254	0.193	0.254	-0.282	-0.419	0.000
9	A	7	ILE	0	0.153	-0.066	4.077	0.375	0.671	0.001	-0.136	-0.161	0.000
10	A	7	ILE	0	-0.082	0.091	4.144	-0.138	-0.031	-0.001	-0.025	-0.080	0.000
11	A	8	GLN	0	0.150	-0.070	6.141	0.177	0.177	0.000	0.000	0.000	0.000
12	A	8	GLN	0	-0.093	0.088	7.422	-0.042	-0.042	0.000	0.000	0.000	0.000
13	A	9	LYS	0	0.000	-0.111	7.295	0.070	0.070	0.000	0.000	0.000	0.000
14	A	9	LYS	1	0.842	1.026	5.916	-0.691	-0.691	0.000	0.000	0.000	0.000
15	A	10	GLU	0	0.159	-0.052	8.429	0.089	0.089	0.000	0.000	0.000	0.000
16	A	10	GLU	-1	-0.939	-0.798	7.599	-0.561	-0.561	0.000	0.000	0.000	0.000
17	A	11	VAL	0	0.080	-0.101	10.080	0.045	0.045	0.000	0.000	0.000	0.000
18	A	11	VAL	0	-0.101	0.087	10.172	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	12	SER	0	0.034	-0.104	11.763	0.009	0.009	0.000	0.000	0.000	0.000
20	A	12	SER	0	-0.063	0.049	11.846	0.031	0.031	0.000	0.000	0.000	0.000
21	A	13	GLU	0	0.101	-0.089	12.929	0.022	0.022	0.000	0.000	0.000	0.000
22	A	13	GLU	-1	-1.030	-0.845	13.097	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	14	ILE	0	0.099	-0.078	14.381	0.026	0.026	0.000	0.000	0.000	0.000
24	A	14	ILE	0	-0.086	0.087	13.098	-0.005	-0.005	0.000	0.000	0.000	0.000
25	A	15	LEU	0	0.090	-0.098	15.965	0.007	0.007	0.000	0.000	0.000	0.000
26	A	15	LEU	0	-0.129	0.084	16.647	0.003	0.003	0.000	0.000	0.000	0.000
27	A	16	SER	0	-0.026	-0.119	17.547	0.003	0.003	0.000	0.000	0.000	0.000
28	A	16	SER	0	-0.026	0.079	17.794	0.012	0.012	0.000	0.000	0.000	0.000
29	A	17	ASP	0	0.129	-0.115	18.902	0.010	0.010	0.000	0.000	0.000	0.000
30	A	17	ASP	-1	-0.984	-0.814	19.123	-0.033	-0.033	0.000	0.000	0.000	0.000
31	A	18	GLN	0	0.127	-0.088	20.327	0.002	0.002	0.000	0.000	0.000	0.000
32	A	18	GLN	0	-0.130	0.087	20.519	0.007	0.007	0.000	0.000	0.000	0.000
33	A	19	LYS	0	-0.045	-0.149	22.184	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	19	LYS	1	0.807	1.029	21.365	0.054	0.054	0.000	0.000	0.000	0.000
35	A	20	SER	0	0.063	-0.043	23.961	0.002	0.002	0.000	0.000	0.000	0.000
36	A	20	SER	0	0.012	0.088	23.629	-0.002	-0.002	0.000	0.000	0.000	0.000
37	A	21	MET	0	0.130	-0.077	24.814	0.005	0.005	0.000	0.000	0.000	0.000
38	A	21	MET	0	-0.082	0.099	23.489	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	22	LYS	0	0.115	-0.056	26.287	0.000	0.000	0.000	0.000	0.000	0.000
40	A	22	LYS	1	0.855	1.045	26.803	0.044	0.044	0.000	0.000	0.000	0.000
41	A	23	ALA	0	0.070	-0.119	28.219	-0.001	-0.001	0.000	0.000	0.000	0.000
42	A	23	ALA	0	-0.090	0.106	29.199	0.001	0.001	0.000	0.000	0.000	0.000
43	A	24	ASP	0	0.102	-0.115	29.597	0.003	0.003	0.000	0.000	0.000	0.000
44	A	24	ASP	-1	-1.008	-0.836	28.920	-0.018	-0.018	0.000	0.000	0.000	0.000
45	A	25	ILE	0	0.077	-0.085	30.429	0.002	0.002	0.000	0.000	0.000	0.000
46	A	25	ILE	0	-0.102	0.079	28.452	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	26	LYS	0	0.079	-0.079	32.102	-0.001	-0.001	0.000	0.000	0.000	0.000
48	A	26	LYS	1	0.709	0.953	33.109	0.012	0.012	0.000	0.000	0.000	0.000
49	A	27	ALA	0	0.112	-0.105	34.069	0.000	0.000	0.000	0.000	0.000	0.000
50	A	27	ALA	0	-0.072	0.109	34.646	0.001	0.001	0.000	0.000	0.000	0.000
51	A	28	ILE	0	0.079	-0.087	35.074	0.003	0.003	0.000	0.000	0.000	0.000
52	A	28	ILE	0	-0.107	0.087	33.064	-0.001	-0.001	0.000	0.000	0.000	0.000
53	A	29	LEU	0	0.069	-0.106	36.267	0.001	0.001	0.000	0.000	0.000	0.000
54	A	29	LEU	0	-0.094	0.079	35.038	-0.001	-0.001	0.000	0.000	0.000	0.000
55	A	30	GLU	0	0.138	-0.081	38.139	0.000	0.000	0.000	0.000	0.000	0.000
56	A	30	GLU	-1	-0.933	-0.785	38.838	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	31	LEU	0	0.099	-0.090	39.685	0.002	0.002	0.000	0.000	0.000	0.000
58	A	31	LEU	0	-0.111	0.096	39.953	0.000	0.000	0.000	0.000	0.000	0.000
59	A	32	LEU	0	0.034	-0.114	40.733	0.002	0.002	0.000	0.000	0.000	0.000
60	A	32	LEU	0	-0.096	0.087	38.999	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	33	GLY	0	-0.024	-0.119	42.155	0.000	0.000	0.000	0.000	0.000	0.000
62	A	34	SER	0	0.044	0.001	44.058	0.000	0.000	0.000	0.000	0.000	0.000
63	A	34	SER	0	-0.085	0.054	43.889	0.001	0.001	0.000	0.000	0.000	0.000
64	A	35	GLN	0	0.032	-0.097	45.891	0.002	0.002	0.000	0.000	0.000	0.000
65	A	35	GLN	0	-0.127	0.077	44.794	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	36	ASN	0	0.053	-0.060	47.744	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	36	ASN	0	-0.109	0.053	52.275	0.000	0.000	0.000	0.000	0.000	0.000
68	A	37	PRO	0	0.012	-0.108	50.897	-0.001	-0.001	0.000	0.000	0.000	0.000
69	A	38	ILE	0	0.130	0.021	51.313	0.001	0.001	0.000	0.000	0.000	0.000
70	A	38	ILE	0	-0.071	0.105	48.617	0.000	0.000	0.000	0.000	0.000	0.000
71	A	39	LYS	0	0.076	-0.067	52.833	0.001	0.001	0.000	0.000	0.000	0.000
72	A	39	LYS	1	0.876	1.052	53.662	0.020	0.020	0.000	0.000	0.000	0.000
73	A	40	GLU	0	0.220	-0.068	55.760	0.001	0.001	0.000	0.000	0.000	0.000
74	A	40	GLU	-1	-0.951	-0.814	55.608	-0.013	-0.013	0.000	0.000	0.000	0.000
75	A	41	SER	0	0.061	-0.064	55.455	0.001	0.001	0.000	0.000	0.000	0.000
76	A	41	SER	0	-0.031	0.065	54.235	0.000	0.000	0.000	0.000	0.000	0.000
77	A	42	LEU	0	0.021	-0.101	56.786	0.001	0.001	0.000	0.000	0.000	0.000
78	A	42	LEU	0	-0.110	0.087	55.509	0.000	0.000	0.000	0.000	0.000	0.000
79	A	43	GLU	0	0.091	-0.115	58.637	0.001	0.001	0.000	0.000	0.000	0.000
80	A	43	GLU	-1	-0.982	-0.843	59.196	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	44	THR	0	0.000	-0.108	60.447	0.000	0.000	0.000	0.000	0.000	0.000
82	A	44	THR	0	-0.054	0.067	59.451	0.000	0.000	0.000	0.000	0.000	0.000
83	A	45	VAL	0	0.109	-0.086	60.733	0.001	0.001	0.000	0.000	0.000	0.000
84	A	45	VAL	0	-0.084	0.105	59.090	0.000	0.000	0.000	0.000	0.000	0.000
85	A	46	ALA	0	0.105	-0.112	62.083	0.001	0.001	0.000	0.000	0.000	0.000
86	A	46	ALA	0	-0.071	0.110	63.156	0.000	0.000	0.000	0.000	0.000	0.000
87	A	47	ALA	0	0.084	-0.103	64.361	0.000	0.000	0.000	0.000	0.000	0.000
88	A	47	ALA	0	-0.070	0.110	65.376	0.000	0.000	0.000	0.000	0.000	0.000
89	A	48	LYS	0	0.067	-0.099	65.342	0.000	0.000	0.000	0.000	0.000	0.000
90	A	48	LYS	1	0.728	1.001	64.740	0.005	0.005	0.000	0.000	0.000	0.000
91	A	49	ILE	0	0.088	-0.102	66.138	0.001	0.001	0.000	0.000	0.000	0.000
92	A	49	ILE	0	-0.089	0.098	63.724	0.000	0.000	0.000	0.000	0.000	0.000
93	A	50	VAL	0	0.073	-0.131	67.723	0.001	0.001	0.000	0.000	0.000	0.000
94	A	50	VAL	0	-0.070	0.123	68.705	0.000	0.000	0.000	0.000	0.000	0.000
95	A	51	ASN	0	0.145	-0.022	69.946	0.000	0.000	0.000	0.000	0.000	0.000
96	A	51	ASN	0	-0.150	0.040	69.834	0.000	0.000	0.000	0.000	0.000	0.000
97	A	52	ASP	0	0.070	-0.101	70.742	0.000	0.000	0.000	0.000	0.000	0.000
98	A	52	ASP	-1	-0.881	-0.794	70.066	-0.005	-0.005	0.000	0.000	0.000	0.000
99	A	53	LEU	0	0.064	-0.104	71.967	0.000	0.000	0.000	0.000	0.000	0.000
100	A	53	LEU	0	-0.064	0.101	70.478	0.000	0.000	0.000	0.000	0.000	0.000
101	A	54	THR	0	0.077	-0.078	73.804	0.000	0.000	0.000	0.000	0.000	0.000
102	A	54	THR	0	-0.079	0.038	74.017	0.000	0.000	0.000	0.000	0.000	0.000
103	A	55	LYS	0	0.039	-0.075	75.711	0.000	0.000	0.000	0.000	0.000	0.000
104	A	55	LYS	1	0.803	1.027	73.079	0.005	0.005	0.000	0.000	0.000	0.000
105	A	56	LEU	0	0.177	-0.061	76.576	0.000	0.000	0.000	0.000	0.000	0.000
106	A	56	LEU	0	-0.127	0.089	75.659	0.000	0.000	0.000	0.000	0.000	0.000
107	A	57	ILE	0	0.037	-0.110	78.091	0.000	0.000	0.000	0.000	0.000	0.000
108	A	57	ILE	0	-0.123	0.081	77.578	0.000	0.000	0.000	0.000	0.000	0.000
109	A	58	ASN	0	0.138	-0.044	79.976	0.000	0.000	0.000	0.000	0.000	0.000
110	A	58	ASN	0	-0.139	0.038	79.897	0.000	0.000	0.000	0.000	0.000	0.000
111	A	59	ASP	0	0.096	-0.086	81.344	0.000	0.000	0.000	0.000	0.000	0.000
112	A	59	ASP	-1	-1.004	-0.867	80.472	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	60	CYS	0	0.002	-0.132	83.138	0.000	0.000	0.000	0.000	0.000	0.000
114	A	60	CYS	0	-0.173	0.076	85.075	0.000	0.000	0.000	0.000	0.000	0.000
115	A	61	PRO	0	0.049	-0.111	81.677	0.000	0.000	0.000	0.000	0.000	0.000
116	A	62	CYS	0	0.090	-0.027	85.022	0.000	0.000	0.000	0.000	0.000	0.000
117	A	62	CYS	0	-0.077	0.116	84.762	0.000	0.000	0.000	0.000	0.000	0.000
118	A	63	ASN	0	0.102	-0.068	86.984	0.000	0.000	0.000	0.000	0.000	0.000
119	A	63	ASN	0	-0.108	0.074	88.623	0.000	0.000	0.000	0.000	0.000	0.000
120	A	64	LYS	0	0.049	-0.080	89.728	0.000	0.000	0.000	0.000	0.000	0.000
121	A	64	LYS	1	0.903	1.074	88.814	0.002	0.002	0.000	0.000	0.000	0.000
122	A	65	GLU	0	0.225	-0.075	91.019	0.000	0.000	0.000	0.000	0.000	0.000
123	A	65	GLU	-1	-1.034	-0.840	90.044	-0.003	-0.003	0.000	0.000	0.000	0.000
124	A	66	ILE	0	0.056	-0.096	92.306	0.000	0.000	0.000	0.000	0.000	0.000
125	A	66	ILE	0	-0.091	0.085	90.203	0.000	0.000	0.000	0.000	0.000	0.000
126	A	67	LEU	0	0.073	-0.100	93.997	0.000	0.000	0.000	0.000	0.000	0.000
127	A	67	LEU	0	-0.111	0.079	93.259	0.000	0.000	0.000	0.000	0.000	0.000
128	A	68	GLU	0	0.088	-0.114	95.550	0.000	0.000	0.000	0.000	0.000	0.000
129	A	68	GLU	-1	-1.004	-0.856	93.990	-0.002	-0.002	0.000	0.000	0.000	0.000
130	A	69	ALA	0	0.086	-0.101	96.787	0.000	0.000	0.000	0.000	0.000	0.000
131	A	69	ALA	0	-0.091	0.102	97.044	0.000	0.000	0.000	0.000	0.000	0.000
132	A	70	LEU	0	-0.019	-0.140	98.320	0.000	0.000	0.000	0.000	0.000	0.000
133	A	70	LEU	0	-0.105	0.092	96.969	0.000	0.000	0.000	0.000	0.000	0.000
134	A	71	GLY	0	-0.012	-0.090	100.167	0.000	0.000	0.000	0.000	0.000	0.000
135	A	72	THR	0	-0.158	-0.099	98.774	0.000	0.000	0.000	0.000	0.000	0.000
136	A	72	THR	0	0.044	0.049	97.543	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:ASN)